ANYL 302 |
| Enzymes such as trypsin and subtilisin are now widely used as efficient catalysts in nonaqueous solvents. The use of redox enzymes is much less widespread, mainly due to their instability which arises from the need for an exogeneous oxidant, typically hydrogen or alkyl peroxides. We have investigated the electrochemistry of a range of haem proteins; microperoxidase, cyclodextrin-modified microperoxidase, cytochrome c, myoglobin, haemoglobin and horseradish peroxidase in nonaqueous solvents. Small changes in the redox potential of a protein can mask substantial changes in ΔH° and ΔS°. These changes appear to be a result of conformational changes in the structure of the protein, which are also affected by the ligation state of the haem. Using resonance Raman and circular dichroism, we have investigated the effect of nonaqueous solvents on the conformation of the protein upon reduction. |
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Analytical Approaches: Sensors
8:30 AM-11:50 AM, Thursday, 14 September 2006 Moscone Center -- Room 123, Oral
Division of Analytical Chemistry |